Type I chaperonins: Not all are created equal

Galit Levy-Rimler, Rachel E. Bell, Nir Ben-Tal, Abdussalam Azem*

*Corresponding author for this work

Research output: Contribution to journalShort surveypeer-review

65 Scopus citations


Type I chaperonins play an essential role in the folding of newly translated and stress-denatured proteins in eubacteria, mitochondria and chloroplasts. Since their discovery, the bacterial chaperonins have provided an excellent model system for investigating the mechanism by which chaperonins mediate protein folding. Due to the high conservation of the primary sequence among Type I chaperonins, it is generally accepted that organellar chaperonins function similar to the bacterial ones. However, recent studies indicate that the chloroplast and mitochondrial chaperonins possess unique structural and functional properties that distinguish them from their bacterial homologs. This review focuses on the unique properties of organellar chaperonins.

Original languageEnglish
Pages (from-to)1-5
Number of pages5
JournalFEBS Letters
Issue number1
StatePublished - 2 Oct 2002


FundersFunder number
German-Israeli Foundation for Scientific Research and Development
United States-Israel Binational Science Foundation


    • Chaperonin
    • GroEL
    • GroES
    • Type I chaperonin
    • cpn10
    • cpn60


    Dive into the research topics of 'Type I chaperonins: Not all are created equal'. Together they form a unique fingerprint.

    Cite this